ID   PBP2_STRP2              Reviewed;         680 AA.
AC   A0A0H2ZQ75;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 2.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Penicillin-binding protein 2B;
DE            Short=PBP2b {ECO:0000303|PubMed:26933838};
GN   Name=penA {ECO:0000303|PubMed:17041037}; Synonyms=pbp2b;
GN   OrderedLocusNames=SPD_1486;
OS   Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=373153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D39 / NCTC 7466;
RX   PubMed=17041037; DOI=10.1128/jb.01148-06;
RA   Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA   Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT   "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT   pneumoniae and comparison with that of unencapsulated laboratory strain
RT   R6.";
RL   J. Bacteriol. 189:38-51(2007).
RN   [2]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=D39 / NCTC 7466;
RX   PubMed=26933838; DOI=10.1111/mmi.13366;
RA   Tsui H.T., Zheng J.J., Magallon A.N., Ryan J.D., Yunck R., Rued B.E.,
RA   Bernhardt T.G., Winkler M.E.;
RT   "Suppression of a deletion mutation in the gene encoding essential PBP2b
RT   reveals a new lytic transglycosylase involved in peripheral peptidoglycan
RT   synthesis in Streptococcus pneumoniae D39.";
RL   Mol. Microbiol. 100:1039-1065(2016).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=D39 / NCTC 7466;
RX   PubMed=28941257; DOI=10.1111/mmi.13847;
RA   Zheng J.J., Perez A.J., Tsui H.T., Massidda O., Winkler M.E.;
RT   "Absence of the KhpA and KhpB (JAG/EloR) RNA-binding proteins suppresses
RT   the requirement for PBP2b by overproduction of FtsA in Streptococcus
RT   pneumoniae D39.";
RL   Mol. Microbiol. 106:793-814(2017).
CC   -!- FUNCTION: A transpeptidase that forms peptide cross-links between
CC       adjacent glycan strands in cell wall peptidoglycan (PG). Part of the
CC       elongasome machinery that synthesizes peripheral PG.
CC       {ECO:0000305|PubMed:28941257}.
CC   -!- SUBUNIT: Interacts with MreC in the elongasome.
CC       {ECO:0000250|UniProtKB:P0A3M6}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:28941257};
CC       Single-pass membrane protein {ECO:0000255}. Note=Localizes to the
CC       midcell division sites, colocalizes with StkP.
CC       {ECO:0000269|PubMed:28941257}.
CC   -!- DISRUPTION PHENOTYPE: Essential, it cannot be disrupted; however
CC       suppressors of the deletion can be isolated under certain growth
CC       conditions. {ECO:0000269|PubMed:26933838, ECO:0000269|PubMed:28941257}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABJ55452.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000410; ABJ55452.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001829432.1; NC_008533.2.
DR   SMR; A0A0H2ZQ75; -.
DR   STRING; 373153.SPD_1486; -.
DR   EnsemblBacteria; ABJ55452; ABJ55452; SPD_1486.
DR   GeneID; 60234391; -.
DR   KEGG; spd:SPD_1486; -.
DR   eggNOG; COG0768; Bacteria.
DR   HOGENOM; CLU_009289_7_0_9; -.
DR   OMA; TLACKTG; -.
DR   BioCyc; SPNE373153:G1G6V-1602-MON; -.
DR   Proteomes; UP000001452; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; -; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR005311; PBP_dimer.
DR   InterPro; IPR036138; PBP_dimer_sf.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56519; SSF56519; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cell shape; Cell wall biogenesis/degradation; Membrane;
KW   Peptidoglycan synthesis; Transmembrane; Transmembrane helix.
FT   CHAIN           1..680
FT                   /note="Penicillin-binding protein 2B"
FT                   /id="PRO_0000454545"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..680
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        386
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AD65"
SQ   SEQUENCE   680 AA;  73873 MW;  56BF2C1AA9B54C3B CRC64;
     MRKFNSHSIP IRLNLLFSIV ILLFMTIIGR LLYMQVLNKD FYEKKLASAS QTKITSSSAR
     GEIYDASGKP LVENTLKQVV SFTRSNKMTA TDLKETAKKL LTYVSISSPN LTERQLADYY
     LADPEIYKKI VEALPSEKRL DSDGNRLSES ELYNNAVDSV QTSQLNYTED EKKEIYLFSQ
     LNAVGNFATG TIATDPLNDS QVAVIASISK EMPGISISTS WDRKVLETSL SSIVGSVSSE
     KAGLPAEEAE AYLKKGYSLN DRVGTSYLEK QYEETLQGKR SVKEIHLDKY GNMESVDTIE
     EGSKGNNIKL TIDLAFQDSV DALLKSYFNS ELENGGAKYS EGVYAVALNP KTGAVLSMSG
     IKHDLKTGEL TPDSLGTVTN VFVPGSVVKA ATISSGWENG VLSGNQTLTD QSIVFQGSAP
     INSWYTQAYG SFPITAVQAL EYSSNTYMVQ TALGLMGQTY QPNMFVGTSN LESAMEKLRS
     TFGEYGLGTA TGIDLPDEST GFVPKEYSFA NYITNAFGQF DNYTPMQLAQ YVATIANNGV
     RVAPRIVEGI YGNNDKGGLG DLIQQLQPTE MNKVNISDSD MSILHQGFYQ VAHGTSGLTT
     GRAFSNGALV SISGKTGTAE SYVADGQQAT NTNAVAYAPS DNPQIAVAVV FPHNTNLTNG
     VGPSIARDII NLYQKYHPMN